ArticleLangmuir : the ACS journal of surfaces and colloids2022
Binding of Cholera Toxin B-Subunit to a Ganglioside GM1-Functionalized PEG-Tethered Lipid Membrane.
Article in Langmuir : the ACS journal of surfaces and colloids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 2 citations in OpenAlex.
- Cholera toxin as a model ABArchives of toxicology · 2026Review
- Linear Reciprocating Tribometer for In Situ Neutron Reflectometry of Soft Matter.Tribology letters · 2025Article
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
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Abstract
We report neutron reflectometry (NR) studies of polyethylene glycol (PEG)-tethered model lipid membranes at the solid-liquid interface and of cholera toxin's B-subunit (CTxB) binding to tethered membranes containing ganglioside GM1 receptors. First, tethered polymer brushes were formed by grafting silane-functionalized PEG lipopolymers to quartz from solution. Subsequent deposition of lipids by Langmuir-Blodgett/Langmuir-Schaefer (LB/LS) resulted in a tethered bilayer structure separated from the solid support by a hydrated PEG layer. NR revealed that the tethers formed a highly hydrated polymer brush, uniformly separating the bilayer from the underlying solid substrate. Further, the lipid bilayer did not significantly perturb the brush's conformation relative to a free brush. Biological functionality of the tethered bilayers was verified by interacting CTxB, with ganglioside GM1 receptors incorporated into the bilayer. The surface coverage of CTxB bound to the lipid membrane, θ
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